Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics.
Saved in:
| Title: | Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics. |
|---|---|
| Authors: | Prokopijevic, Milos1, Prodanovic, Olivera1, Spasojevic, Dragica1, Stojanovic, Zeljko2, Radotic, Ksenija1, Prodanovic, Radivoje3 rprodano@chem.bg.ac.rs |
| Source: | Bioprocess & Biosystems Engineering. May2014, Vol. 37 Issue 5, p799-804. 6p. |
| Subjects: | Soy bran, Glycidyl methacrylate, Peroxidase, Glutaraldehyde, Ethylene glycol, Enzyme analysis, High temperatures |
| Abstract: | Soybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents. [ABSTRACT FROM AUTHOR] |
| Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Links: – Type: pdflink Text: Availability: 0 |
|---|---|
| Header | DbId: egs DbLabel: Engineering Source An: 95660196 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
| IllustrationInfo | |
| Items | – Name: Title Label: Title Group: Ti Data: Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Prokopijevic%2C+Milos%22">Prokopijevic, Milos</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Prodanovic%2C+Olivera%22">Prodanovic, Olivera</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Spasojevic%2C+Dragica%22">Spasojevic, Dragica</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Stojanovic%2C+Zeljko%22">Stojanovic, Zeljko</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Radotic%2C+Ksenija%22">Radotic, Ksenija</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Prodanovic%2C+Radivoje%22">Prodanovic, Radivoje</searchLink><relatesTo>3</relatesTo><i> rprodano@chem.bg.ac.rs</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Bioprocess+%26+Biosystems+Engineering%22">Bioprocess & Biosystems Engineering</searchLink>. May2014, Vol. 37 Issue 5, p799-804. 6p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Soy+bran%22">Soy bran</searchLink><br /><searchLink fieldCode="DE" term="%22Glycidyl+methacrylate%22">Glycidyl methacrylate</searchLink><br /><searchLink fieldCode="DE" term="%22Peroxidase%22">Peroxidase</searchLink><br /><searchLink fieldCode="DE" term="%22Glutaraldehyde%22">Glutaraldehyde</searchLink><br /><searchLink fieldCode="DE" term="%22Ethylene+glycol%22">Ethylene glycol</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+analysis%22">Enzyme analysis</searchLink><br /><searchLink fieldCode="DE" term="%22High+temperatures%22">High temperatures</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Soybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=95660196 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1007/s00449-013-1050-z Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 6 StartPage: 799 Subjects: – SubjectFull: Soy bran Type: general – SubjectFull: Glycidyl methacrylate Type: general – SubjectFull: Peroxidase Type: general – SubjectFull: Glutaraldehyde Type: general – SubjectFull: Ethylene glycol Type: general – SubjectFull: Enzyme analysis Type: general – SubjectFull: High temperatures Type: general Titles: – TitleFull: Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Prokopijevic, Milos – PersonEntity: Name: NameFull: Prodanovic, Olivera – PersonEntity: Name: NameFull: Spasojevic, Dragica – PersonEntity: Name: NameFull: Stojanovic, Zeljko – PersonEntity: Name: NameFull: Radotic, Ksenija – PersonEntity: Name: NameFull: Prodanovic, Radivoje IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 05 Text: May2014 Type: published Y: 2014 Identifiers: – Type: issn-print Value: 16157591 Numbering: – Type: volume Value: 37 – Type: issue Value: 5 Titles: – TitleFull: Bioprocess & Biosystems Engineering Type: main |
| ResultId | 1 |